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CYOE_YERE8
ID   CYOE_YERE8              Reviewed;         296 AA.
AC   A1JNP6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Protoheme IX farnesyltransferase {ECO:0000255|HAMAP-Rule:MF_00154};
DE            EC=2.5.1.141 {ECO:0000255|HAMAP-Rule:MF_00154};
DE   AltName: Full=Heme B farnesyltransferase {ECO:0000255|HAMAP-Rule:MF_00154};
DE   AltName: Full=Heme O synthase {ECO:0000255|HAMAP-Rule:MF_00154};
GN   Name=cyoE {ECO:0000255|HAMAP-Rule:MF_00154}; OrderedLocusNames=YE3145;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Converts heme B (protoheme IX) to heme O by substitution of
CC       the vinyl group on carbon 2 of heme B porphyrin ring with a
CC       hydroxyethyl farnesyl side group. {ECO:0000255|HAMAP-Rule:MF_00154}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate +
CC         Fe(II)-heme o; Xref=Rhea:RHEA:28070, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:60344, ChEBI:CHEBI:60530,
CC         ChEBI:CHEBI:175763; EC=2.5.1.141; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00154};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; heme O biosynthesis;
CC       heme O from protoheme: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00154}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00154}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00154}.
CC   -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC       according to the Fischer nomenclature. {ECO:0000255|HAMAP-
CC       Rule:MF_00154}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. Protoheme IX
CC       farnesyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_00154}.
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DR   EMBL; AM286415; CAL13180.1; -; Genomic_DNA.
DR   RefSeq; YP_001007327.1; NC_008800.1.
DR   AlphaFoldDB; A1JNP6; -.
DR   SMR; A1JNP6; -.
DR   STRING; 393305.YE3145; -.
DR   EnsemblBacteria; CAL13180; CAL13180; YE3145.
DR   KEGG; yen:YE3145; -.
DR   PATRIC; fig|393305.7.peg.3349; -.
DR   eggNOG; COG0109; Bacteria.
DR   HOGENOM; CLU_029631_0_0_6; -.
DR   OMA; QFFWQFP; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008495; F:protoheme IX farnesyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048034; P:heme O biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd13957; PT_UbiA_Cox10; 1.
DR   Gene3D; 1.10.357.140; -; 1.
DR   HAMAP; MF_00154; CyoE_CtaB; 1.
DR   InterPro; IPR006369; Protohaem_IX_farnesylTrfase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR   InterPro; IPR044878; UbiA_sf.
DR   PANTHER; PTHR43448; PTHR43448; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
DR   PROSITE; PS00943; UBIA; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Heme biosynthesis; Membrane;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..296
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000326977"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ   SEQUENCE   296 AA;  32252 MW;  3B3AEBCE69496B7F CRC64;
     MMIKQYLQVT KPGIIFGNLI SVVGGFLLAS KGVIDYPLFL ATLFGVSLVV ASGCVFNNYI
     DRDIDRIMER TKNRVLVKGL IDPKVSLIYA SILGIAGMLL LYVGANPLAM WLAVIGFVIY
     VGVYSLYMKR KSVYGTLIGS LSGAAPPVIG YCAVTGQFDM GALILLLIFS LWQMPHSYAI
     AIFRFKDYQA ANIPVLPVIK GISVTKNHIT LYILAFMVAT LMLTLSGYAG YKYLVVAAAV
     SVWWLGMALR GYKATNDSVW ARKLFVFSII AITSLSVMMS VDFNVPSSAG LLTYVG
 
 
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